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Crystal structure and function of C-terminal Sau3AI domain
- Source :
-
BBA - Proteins & Proteomics . Jan2009, Vol. 1794 Issue 1, p118-123. 6p. - Publication Year :
- 2009
-
Abstract
- Abstract: Sau3AI is a type II restriction enzyme that recognizes the 5′-GATC-3′ sequence in double-strand DNA and cleaves at 5′ to the G residue. The C-terminal domain of Sau3AI (Sau3AI-C), which contains amino acids from 233 to 489, was crystallized and its structure was solved by using the Multi-wavelength Anomalous Diffraction method. The Sau3AI-C structure at 1.9 Å resolution is similar to the structure of MutH, a DNA mismatch repair protein that shares high sequence similarity with the N-terminal Sau3AI domain. The functional analysis shows that Sau3AI-C can bind DNA with one recognition sequence but has no cleavage activity. These results indicate that Sau3AI is a pseudo-dimer belonging to the type IIe restriction enzymes and the Sau3AI-C is the allosteric effector domain that assists DNA binding and cleavage. [Copyright &y& Elsevier]
Details
- Language :
- English
- ISSN :
- 15709639
- Volume :
- 1794
- Issue :
- 1
- Database :
- Academic Search Index
- Journal :
- BBA - Proteins & Proteomics
- Publication Type :
- Academic Journal
- Accession number :
- 35507461
- Full Text :
- https://doi.org/10.1016/j.bbapap.2008.09.008